dBET57 - CAS 1883863-52-2

dBET57 is a potent and selective degrader of BRD4BD1 based on the PROTAC technology. dBET57 mediates recruitment to the CRL4CRBN E3 ubiquitin ligase, with a DC50/5h of 500 nM for BRD4BD1, and is inactive on BRD4BD2.

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Molecular Formula
Molecular Weight


    • Specification
      • Purity
        Soluble in DMSO
        Solid Powder
        Store at 2-8°C for short term (days to weeks) or -20°C for long term (months to years)
        Room temperature in continental US; may vary elsewhere
        IUPAC Name
        dBET 57; dBET-57; 6H-Thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepine-6-acetamide, 4-(4-chlorophenyl)-N-[2-[[2-(2,6-dioxo-3-piperidinyl)-2,3-dihydro-1,3-dioxo-1H-isoindol-4-yl]amino]ethyl]-2,3,9-trimethyl-, (6S)-; 2-[(6S)-4-(4-Chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl]-N-(2-{[2-(2,6-dioxo-3-piperidinyl)-1,3-dioxo-2,3-dihydro-1H-isoindol-4-yl]amino}ethyl)acetamide
    • Properties
      • Density
        1.60±0.1 g/cm3 (Predicted)
        InChI Key
        Canonical SMILES
    • Reference Reading
      • 1. Plasticity in binding confers selectivity in ligand-induced protein degradation.
        Nowak, R.P., DeAngelo, S.L., Buckley, D., He, Z., Donovan, K.A., An, J., Safaee, N., Jedrychowski, M.P., Ponthier, C.M., Ishoey, M. and Zhang, T., 2018. Nature chemical biology, 14(7), pp.706-714.
        Heterobifunctional small-molecule degraders that induce protein degradation through ligase-mediated ubiquitination have shown considerable promise as a new pharmacological modality. However, we currently lack a detailed understanding of the molecular basis for target recruitment and selectivity, which is critically required to enable rational design of degraders. Here we utilize a comprehensive characterization of the ligand-dependent CRBN-BRD4 interaction to demonstrate that binding between proteins that have not evolved to interact is plastic. Multiple X-ray crystal structures show that plasticity results in several distinct low-energy binding conformations that are selectively bound by ligands. We demonstrate that computational protein-protein docking can reveal the underlying interprotein contacts and inform the design of a BRD4 selective degrader that can discriminate between highly homologous BET bromodomains. Our findings that plastic interprotein contacts confer selectivity for ligand-induced protein dimerization provide a conceptual framework for the development of heterobifunctional ligands.
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